A series of point mutations reveal interactions between the calcium-binding sites of calmodulin

Author:

Starovasnik Melissa A.,Klevit Rachel E.,Su Dai-Rong,Beckingham Kathy

Funder

NIH

helth Association Established Investigatorship

National Science Foundation Predoctoral Fellowship

Public Health Service

National Science Foundation

Advanced Research/Advanced Technology

Program of the Texas Higher Education Board

the Welch Foundation of Texas

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference34 articles.

1. Cadmium-113 nuclear magnetic resonance studies of proteolytic fragments of calmodulin: Assignment of strong and weak cation binding sites;Andersson;Biochemistry,1983

2. Ring-current effects and magnetic anisotropy effects of carbonyl groups on the α-CH proton chemical shifts of the basic pancreatic trypsin inhibitor and tendamistat;Asakura;J. Mag. Res.,1991

3. Structure of calmodulin refined at 2.2 Å resolution;Babu;J. Mol. Biol.,1988

4. Three-dimensional structure of calmodulin;Babu;Nature,1985

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